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Protein

Catalase

Gene

katA

Organism
Proteus mirabilis
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Decomposes hydrogen peroxide into water and oxygen; serves to protect cells from the toxic effects of hydrogen peroxide.

Catalytic activityi

2 H2O2 = O2 + 2 H2O.PROSITE-ProRule annotation

Cofactori

Protein has several cofactor binding sites:

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei54 – 541
Active sitei127 – 1271
Metal bindingi337 – 3371Iron (heme axial ligand)1 Publication

GO - Molecular functioni

  1. catalase activity Source: UniProtKB-EC
  2. heme binding Source: InterPro
  3. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. hydrogen peroxide catabolic process Source: UniProtKB-KW
  2. response to oxidative stress Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase, Peroxidase

Keywords - Biological processi

Hydrogen peroxide

Keywords - Ligandi

Heme, Iron, Metal-binding, NADP

Enzyme and pathway databases

BRENDAi1.11.1.6. 5044.
SABIO-RKP42321.

Names & Taxonomyi

Protein namesi
Recommended name:
Catalase (EC:1.11.1.6)
Gene namesi
Name:katA
OrganismiProteus mirabilis
Taxonomic identifieri584 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeProteus

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 484484CatalasePRO_0000084992Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei53 – 531Methionine sulfone1 Publication

Keywords - PTMi

Oxidation

Interactioni

Subunit structurei

Homotetramer.

Structurei

Secondary structure

1
484
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi17 – 193Combined sources
Beta strandi22 – 243Combined sources
Helixi34 – 4310Combined sources
Beta strandi52 – 543Combined sources
Beta strandi56 – 6611Combined sources
Turni71 – 733Combined sources
Helixi77 – 793Combined sources
Beta strandi85 – 939Combined sources
Beta strandi95 – 973Combined sources
Beta strandi103 – 1075Combined sources
Beta strandi110 – 1178Combined sources
Beta strandi120 – 13011Combined sources
Helixi137 – 1393Combined sources
Helixi140 – 1478Combined sources
Turni151 – 1533Combined sources
Helixi158 – 1669Combined sources
Helixi169 – 1713Combined sources
Helixi172 – 1798Combined sources
Helixi181 – 1833Combined sources
Beta strandi184 – 1863Combined sources
Helixi188 – 1903Combined sources
Beta strandi199 – 2024Combined sources
Beta strandi208 – 21710Combined sources
Helixi226 – 23510Combined sources
Helixi239 – 24911Combined sources
Beta strandi255 – 26410Combined sources
Helixi265 – 2695Combined sources
Beta strandi271 – 2733Combined sources
Turni284 – 2863Combined sources
Beta strandi290 – 29910Combined sources
Helixi304 – 3074Combined sources
Turni308 – 3103Combined sources
Helixi328 – 34518Combined sources
Helixi349 – 3513Combined sources
Turni353 – 3553Combined sources
Beta strandi358 – 3603Combined sources
Beta strandi382 – 3843Combined sources
Beta strandi386 – 3883Combined sources
Helixi394 – 3963Combined sources
Helixi412 – 4143Combined sources
Helixi420 – 4289Combined sources
Helixi431 – 44515Combined sources
Helixi450 – 46314Combined sources
Helixi465 – 47814Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1E93X-ray2.00A1-484[»]
1H6NX-ray2.11A1-484[»]
1H7KX-ray2.40A2-484[»]
1M85X-ray2.00A1-484[»]
1MQFX-ray2.50A1-484[»]
1NM0X-ray2.30A1-484[»]
2CAGX-ray2.70A1-484[»]
2CAHX-ray2.70A1-484[»]
3HB6X-ray2.30A1-484[»]
ProteinModelPortaliP42321.
SMRiP42321. Positions 4-479.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP42321.

Family & Domainsi

Sequence similaritiesi

Belongs to the catalase family.Curated

Family and domain databases

Gene3Di2.40.180.10. 1 hit.
InterProiIPR018028. Catalase.
IPR020835. Catalase-like_dom.
IPR024708. Catalase_AS.
IPR024711. Catalase_clade1/3.
IPR011614. Catalase_core.
IPR002226. Catalase_haem_BS.
IPR010582. Catalase_immune_responsive.
[Graphical view]
PANTHERiPTHR11465. PTHR11465. 1 hit.
PfamiPF00199. Catalase. 1 hit.
PF06628. Catalase-rel. 1 hit.
[Graphical view]
PIRSFiPIRSF038928. Catalase_clade1-3. 1 hit.
PRINTSiPR00067. CATALASE.
SMARTiSM01060. Catalase. 1 hit.
[Graphical view]
SUPFAMiSSF56634. SSF56634. 1 hit.
PROSITEiPS00437. CATALASE_1. 1 hit.
PS00438. CATALASE_2. 1 hit.
PS51402. CATALASE_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P42321-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEKKKLTTAA GAPVVDNNNV ITAGPRGPML LQDVWFLEKL AHFDREVIPE
60 70 80 90 100
RRMHAKGSGA FGTFTVTHDI TKYTRAKIFS EVGKKTEMFA RFSTVAGERG
110 120 130 140 150
AADAERDIRG FALKFYTEEG NWDMVGNNTP VFYLRDPLKF PDLNHIVKRD
160 170 180 190 200
PRTNMRNMAY KWDFFSHLPE SLHQLTIDMS DRGLPLSYRF VHGFGSHTYS
210 220 230 240 250
FINKDNERFW VKFHFRCQQG IKNLMDDEAE ALVGKDRESS QRDLFEAIER
260 270 280 290 300
GDYPRWKLQI QIMPEKEAST VPYNPFDLTK VWPHADYPLM DVGYFELNRN
310 320 330 340 350
PDNYFSDVEQ AAFSPANIVP GISFSPDKML QGRLFSYGDA HRYRLGVNHH
360 370 380 390 400
QIPVNAPKCP FHNYHRDGAM RVDGNSGNGI TYEPNSGGVF QEQPDFKEPP
410 420 430 440 450
LSIEGAADHW NHREDEDYFS QPRALYELLS DDEHQRMFAR IAGELSQASK
460 470 480
ETQQRQIDLF TKVHPEYGAG VEKAIKVLEG KDAK
Length:484
Mass (Da):55,614
Last modified:November 1, 1995 - v1
Checksum:iADC25F3CB41F5C50
GO

Mass spectrometryi

Molecular mass is 55643±5 Da from positions 1 - 484. Determined by ESI. 1 Publication

Sequence databases

PIRiA58663.
RefSeqiWP_004248382.1. NZ_KN150749.1.

Genome annotation databases

GeneIDi6802690.

Cross-referencesi

Sequence databases

PIRiA58663.
RefSeqiWP_004248382.1. NZ_KN150749.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1E93X-ray2.00A1-484[»]
1H6NX-ray2.11A1-484[»]
1H7KX-ray2.40A2-484[»]
1M85X-ray2.00A1-484[»]
1MQFX-ray2.50A1-484[»]
1NM0X-ray2.30A1-484[»]
2CAGX-ray2.70A1-484[»]
2CAHX-ray2.70A1-484[»]
3HB6X-ray2.30A1-484[»]
ProteinModelPortaliP42321.
SMRiP42321. Positions 4-479.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi6802690.

Enzyme and pathway databases

BRENDAi1.11.1.6. 5044.
SABIO-RKP42321.

Miscellaneous databases

EvolutionaryTraceiP42321.

Family and domain databases

Gene3Di2.40.180.10. 1 hit.
InterProiIPR018028. Catalase.
IPR020835. Catalase-like_dom.
IPR024708. Catalase_AS.
IPR024711. Catalase_clade1/3.
IPR011614. Catalase_core.
IPR002226. Catalase_haem_BS.
IPR010582. Catalase_immune_responsive.
[Graphical view]
PANTHERiPTHR11465. PTHR11465. 1 hit.
PfamiPF00199. Catalase. 1 hit.
PF06628. Catalase-rel. 1 hit.
[Graphical view]
PIRSFiPIRSF038928. Catalase_clade1-3. 1 hit.
PRINTSiPR00067. CATALASE.
SMARTiSM01060. Catalase. 1 hit.
[Graphical view]
SUPFAMiSSF56634. SSF56634. 1 hit.
PROSITEiPS00437. CATALASE_1. 1 hit.
PS00438. CATALASE_2. 1 hit.
PS51402. CATALASE_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Complete amino acid sequence of Proteus mirabilis PR catalase. Occurrence of a methionine sulfone in the close proximity of the active site."
    Buzy A., Bracchi V., Sterjiades R., Chroboczek J., Thibault P., Gagnon J., Jouve H.-M., Hudry-Clergeon G.
    J. Protein Chem. 14:59-72(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE, NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-305, OXIDATION AT MET-53, MASS SPECTROMETRY.
    Strain: PR.
  2. "Crystal structure of Proteus mirabilis PR catalase with and without bound NADPH."
    Gouet P., Jouve H.-M., Dideberg O.
    J. Mol. Biol. 249:933-954(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
    Strain: PR.
  3. "Ferryl intermediates of catalase captured by time-resolved Weissenberg crystallography and UV-VIS spectroscopy."
    Gouet P., Jouve H.-M., Williams P.A., Andersson I., Andreoletti P., Nussaume L., Hajdu J.
    Nat. Struct. Biol. 3:951-956(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS), ABSORPTION SPECTROSCOPY.
  4. "High-resolution structure and biochemical properties of a recombinant Proteus mirabilis catalase depleted in iron."
    Andreoletti P., Sainz G., Jaquinod M., Gagnon J., Jouve H.-M.
    Proteins 50:261-271(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), EPR SPECTROSCOPY.

Entry informationi

Entry nameiCATA_PROMI
AccessioniPrimary (citable) accession number: P42321
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: April 1, 2015
This is version 95 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.